| AVS 56th International Symposium & Exhibition | |
| Biomaterial Interfaces | Tuesday Sessions |
| Session BI-TuP |
| Session: | Biomaterial Interfaces Poster Session I |
| Presenter: | G. Collier, Clemson University |
| Authors: | G. Collier, Clemson University R.A. Latour, Clemson University S.J. Stuart, Clemson University |
| Correspondent: | Click to Email |
The chemical and physical interactions between proteins and biomaterial surfaces govern the biocompatibility of those materials when introduced into a living system. Therefore, the possibility of controlling biocompatibility on a molecular level through the strategic design of biomaterials begins with the study of these interactions at the atomic level. Without an accurate molecular description of the way that proteins interact with biomaterials, biomaterial design is primarily relegated to a trial-and-error approach. To address this issue, we have begun to evaluate the applicability of existing all-atom molecular simulation methods and force fields to the unique situation of simulating the interaction of structured peptides with solid biomaterial surfaces.
Today's most advanced molecular modeling tools do not include parameterization options for molecular systems interacting with solid biomaterial surfaces, so we have undertaken a variety of pilot studies to guide the development of our methods for use in more complex simulations. These pilot studies include nanosecond-scale simulations of structured peptides interacting with charged and uncharged self-assembled monolayer (SAM) surfaces, ion distributions over a charged SAM surface, peptide-peptide interaction studies, peptide stability studies, analysis of environmental changes resulting from peptide conformation changes, and analysis of the role of water molecules in the peptide-surface adsorption process. The adsorption and stability studies are being conducted using multiple molecular modeling force fields, enabling a comparison of their performance and usefulness in the simulation of these unique systems. The majority of this work has been conducted using replica-exchange molecular dynamics (REMD) techniques in order to optimize conformational sampling, resulting in the most efficient path toward structural data that can be compared with experimental results.
The results from these studies are enabling us to assess the suitability of currently available molecular simulation methods and force fields and are providing us with a better understanding of peptide-surface interactions at the atomic level.